Summary of project PR000921
This data is available at the NIH Common Fund's National Metabolomics Data Repository (NMDR) website, the Metabolomics Workbench, https://www.metabolomicsworkbench.org, where it has been assigned Project ID PR000921. The data can be accessed directly via it's Project DOI: 10.21228/M8N698 This work is supported by NIH grant, U2C- DK119886.
See: https://www.metabolomicsworkbench.org/about/howtocite.php
| Project ID: | PR000921 |
| Project DOI: | doi: 10.21228/M8N698 |
| Project Title: | NMR Metabolomic Analysis of Bacterial Resistance Pathways Using Multivalent Quaternary Ammonium Functionalized Macromolecules |
| Project Type: | NMR Hydrophilic Metabolomic Analysis |
| Project Summary: | Multivalent antimicrobial dendrimers are an exciting new system that is being developed to address the growing problem of drug resistant bacteria. Nuclear Magnetic Resonance (NMR) metabolomics is a quantitative and reproducible method for the determination of bacterial response to environmental stressors and for visualization of perturbations to biochemical pathways. NMR metabolomics is used to elucidate metabolite differences between wild type and antimicrobially mutated Escherichia coli (E. coli) samples. Proton (1H) NMR hydrophilic metabolite analysis was conducted on samples of E. coli after 33 growth cycles of a minimum inhibitory challenge to E. coli by poly(amidoamine) dendrimers functionalized with mannose and with C16-DABCO quaternary ammonium endgroups and compared to the metabolic profile of wild type E. coli. The wild type and mutated E. coli samples were separated into distinct sample sets by hierarchical clustering, principal component analysis (PCA) and sparse partial least squares discriminate analysis (sPLS-DA). Metabolite components of membrane fortification and energy related pathways had a significant p-value and fold change between the wild type and mutated E. coli. Amino acids commonly associated with membrane fortification from cationic antimicrobials, such as lysine, were found to have a higher concentration in the mutated E. coli than the wild type E. coli. N-acetylglucosamine, a major component of peptidoglycan synthesis, was found to have a 25 fold higher concentration in the mid log phase of the mutated E. coli than the mid log phase of the wild type. The metabolic profile suggests that E. coli change their peptidoglycan composition in order to garner protection from the highly positively charged and multivalent C16 DABCO and mannose functionalized dendrimer. |
| Institute: | Montana State University |
| Department: | Chemistry and Biochemistry |
| Laboratory: | Cloninger |
| Last Name: | Aries |
| First Name: | Michelle |
| Address: | Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT, 59717 USA |
| Email: | michelle.aries@montana.edu |
| Phone: | 4069943051 |
Summary of all studies in project PR000921
| Study ID | Study Title | Species | Institute | Analysis(* : Contains Untargted data) | Release Date | Version | Samples | Download(* : Contains raw data) |
|---|---|---|---|---|---|---|---|---|
| ST001351 | NMR Metabolomic Analysis of Bacterial Resistance Pathways Using Multivalent Quaternary Ammonium Functionalized Macromolecules | Escherichia coli | Montana State University | NMR | 2021-04-21 | 1 | 35 | Uploaded data (197.8K) |
